H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH is a proline- and threonine-rich peptide favoring turn and extended-coil structures. Aspartate and lysine introduce an internal salt-bridge potential that shapes local conformation. Researchers investigate its dynamic hydrogen-bonding and solvent dependence. Applications include motif characterization, protein-surface mapping, and peptide-material interface studies.
CAT No: R2568
CAS No:562082-63-7
Synonyms/Alias:H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH;EA2;562082-63-7;HY-P5473;DA-52776;CS-0884124;
H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH is a synthetic peptide characterized by a unique sequence of amino acids, offering valuable properties for diverse biochemical and research applications. Its structural composition, featuring multiple threonine and proline residues interspersed with aspartic acid, serine, alanine, and lysine, enables it to participate in a range of molecular interactions. The presence of both hydrophilic and hydrophobic amino acids in this peptide sequence allows it to adopt flexible conformations, making it suitable for studies investigating peptide folding, stability, and interactions with other biomolecules. Researchers often utilize such peptides to explore fundamental questions in protein science, including the mechanisms of peptide self-assembly, substrate recognition, and the influence of sequence motifs on biological activity. The synthetic nature of H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH ensures consistent quality and reproducibility, which is essential for experimental reliability in laboratory settings.
Peptide Structure-Function Analysis: H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH serves as a valuable tool in the field of structure-function relationships within peptides and proteins. Researchers employ this peptide to dissect the contributions of individual residues or motifs—such as the repeated threonine and proline segments—to overall conformation and biological function. By substituting or modifying specific amino acids, scientists can systematically evaluate how these changes impact folding patterns, stability, or binding affinities with target molecules. The insights gained from such analyses are pivotal for rational peptide design and the development of biomimetic materials.
Molecular Recognition Studies: In studies focused on molecular recognition, this peptide finds use as a model substrate or ligand for analyzing protein-peptide and peptide-peptide interactions. The distinct arrangement of charged, polar, and nonpolar residues allows it to engage in specific binding events with enzymes, receptors, or antibodies. Through techniques such as surface plasmon resonance, isothermal titration calorimetry, or co-crystallization, investigators can characterize the binding kinetics, thermodynamics, and structural determinants that govern these interactions. Such research enhances the understanding of molecular recognition processes central to cellular communication and signal transduction.
Enzyme Substrate Profiling: H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH is frequently employed as a synthetic substrate in enzymology. Its sequence is particularly suitable for studying protease specificity, as the presence of multiple proline and threonine residues can influence cleavage patterns. By monitoring the enzymatic processing of this peptide, researchers can elucidate substrate preferences, reaction mechanisms, and potential regulatory factors affecting enzyme activity. These findings contribute to the broader field of enzyme engineering, where tailored substrates are essential for screening, assay development, and inhibitor discovery.
Biomaterial and Hydrogel Research: The peptide's propensity for self-assembly, driven by its sequence composition, makes it a candidate for biomaterial and hydrogel development. Scientists investigate its ability to form ordered structures or networks, which can be harnessed for creating scaffolds in tissue engineering, drug delivery systems, or cell culture platforms. The versatility of H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH in forming stable, biocompatible matrices is explored through various physical and chemical modifications, expanding its utility in materials science.
Peptide-Based Sensor Development: In the realm of biosensors, this synthetic peptide is integrated into platforms designed to detect specific analytes or environmental changes. By immobilizing it onto sensor surfaces or incorporating it into nanostructured materials, researchers can exploit its binding properties and conformational responsiveness to generate detectable signals. These peptide-based sensors are evaluated for their sensitivity, selectivity, and robustness in applications ranging from environmental monitoring to analytical biochemistry, demonstrating the broad utility of H-Pro-Thr-Thr-Asp-Ser-Thr-Thr-Pro-Ala-Pro-Thr-Thr-Lys-OH across scientific disciplines.
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